Protease-inhibitory activities of leupeptin analogues.

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Abstract
Thirty analogues of leupeptin were synthesized and examined for the their inhibitory activities against trypsin, papain, plasmin, kallikrein, thrombin and urokinase in vitro. Benzoyl-and .alpha.-naphthalenesulfonyl-L-leucyl-L-argininal were 8 times more inhibitory to papain, benzyloxycarbonyl-L-pyroglutamyl-L-leucyl-L-argininal 10 times more to trypsin and plasmin, and DL-2-pipecolyl-L-leucyl-L-argininal 25 times more to kallikrein than leupeptin. Against urokinase, only L-pyroglutamyl-L-leucyl-L-argininal exhibited a potent inhibitory activity. .alpha.-Naphthalenesulfonyl-, dansyl- and benzyloxycarbonyl-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butryl-L-leucyl-L-argininal were inhibitory to thrombin.